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000051336 084__ $$2WoS$$aChemistry, Physical
000051336 084__ $$2WoS$$aPhysics, Atomic, Molecular & Chemical
000051336 1001_ $$0P:(DE-HGF)0$$aHrabakova, J.$$b0
000051336 245__ $$aLong distance electron transfer in cytochrome c oxidase immobilised on electrodes. A surface enhanced resonance Raman spectroscopic study
000051336 260__ $$aCambridge$$bRSC Publ.$$c2006
000051336 300__ $$a759 - 766
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000051336 440_0 $$04916$$aPhysical Chemistry Chemical Physics$$v8$$x1463-9076
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000051336 520__ $$aCytochrome c oxidase was tethered to a functionalised Ag electrode via a histidine-tag on the C-terminus of subunit I or II and embedded in a phospholipid bilayer. The uniformly oriented membrane-bound proteins were studied by surface enhanced resonance Raman spectroscopy (SERRS) that reveals preservation of the native structures of the heme a and heme a(3) sites. On the basis of time-dependent SERRS measurements, the rate constant for the heterogeneous electron transfer to heme a was determined to be 0.002 s(-1) independent of the enzyme orientation and the overpotential. Taking into account that the electrode-to-heme a distance is larger than 50 A, these findings suggest an electron hopping mechanism in which the Cu(A) center is not involved. Electrochemical reduction is restricted to heme a whereas electron transfer from heme a to heme a(3), which in solution occurs on the nanosecond time scale, is drastically slowed down. It may be that the network of cooperativities that links intramolecular electron transfer and proton translocation is perturbed in the immobilised enzyme, possibly due to the effect of the interfacial electric field.
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000051336 650_2 $$2MeSH$$aChemistry, Physical
000051336 650_2 $$2MeSH$$aElectrodes
000051336 650_2 $$2MeSH$$aElectron Transport Complex IV: chemistry
000051336 650_2 $$2MeSH$$aEnzymes, Immobilized: chemistry
000051336 650_2 $$2MeSH$$aModels, Chemical
000051336 650_2 $$2MeSH$$aOxidation-Reduction
000051336 650_2 $$2MeSH$$aPhysicochemical Phenomena
000051336 650_2 $$2MeSH$$aSilver: chemistry
000051336 650_2 $$2MeSH$$aSpectrum Analysis, Raman: methods
000051336 650_2 $$2MeSH$$aSurface Properties
000051336 650_2 $$2MeSH$$aTime Factors
000051336 650_7 $$00$$2NLM Chemicals$$aEnzymes, Immobilized
000051336 650_7 $$07440-22-4$$2NLM Chemicals$$aSilver
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000051336 7001_ $$0P:(DE-Juel1)VDB5396$$aAtaka, K.$$b1$$uFZJ
000051336 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b2$$uFZJ
000051336 7001_ $$0P:(DE-HGF)0$$aHildebrandt, P.$$b3
000051336 7001_ $$0P:(DE-HGF)0$$aMurgida, D.$$b4
000051336 773__ $$0PERI:(DE-600)1476244-4$$a10.1039/b513379n$$gVol. 8, p. 759 - 766$$p759 - 766$$q8<759 - 766$$tPhysical Chemistry Chemical Physics$$v8$$x1463-9076$$y2006
000051336 8567_ $$uhttp://hdl.handle.net/2128/713$$uhttp://dx.doi.org/10.1039/b513379n
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